Plasminogen activator inhibitor 1 RNA-binding protein (SERBP1)
The protein contains 408 amino acids for an estimated molecular weight of 44965 Da.
May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation (PubMed:28695742). (updated: Jan. 16, 2019)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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Biological Process
PML body organization
Regulation of apoptotic process
Regulation of mRNA stability
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Membrane
Nucleus
Perinuclear region of cytoplasm
Plasma membrane
Molecular Function
Cadherin binding
MRNA 3'-UTR binding
Poly(A) RNA binding
Ribosome binding
RNA binding
SUMO binding
The reference OMIM entry for this protein is 607378
Serpine1 mrna-binding protein 1; serbp1
Pai1 rna-binding protein 1
Pairbp1
CLONING
Heaton et al. (2001) purified Pairbp1 from rat hepatoma cells and determined that it binds to the cyclic nucleotide-responsive element of the rat Pai1 gene (173360). Based on homology with the N-terminal amino acid sequence of the rat protein, they identified a human PAIRBP1 cDNA. The deduced 387-amino acid human protein does not contain an RNA recognition motif or a K homology domain, but it has other motifs frequently found in RNA-binding proteins, notably an RGG box, an RG-rich region, and an arg-rich region. It also contains a putative protein kinase A (see 601639) phosphorylation site at ser74. PAIRBP1 shares several blocks of conserved sequence with proteins from Arabidopsis, Drosophila, chicken, mouse, and rat.GENE FUNCTION
Using RNA electrophoretic mobility shift assay and ultraviolet cross-linking experiments, Heaton et al. (2001) determined that recombinant PAIRBP1 binds to the cyclic nucleotide-responsive element of rat Pai1 in a concentration-dependent manner. By mutation analysis, they determined that PAIRBP1 interacts primarily with the adenine-rich region of the response element.MAPPING
Gross (2014) mapped the SERBP1 gene to chromosome 1p31.3 based on an alignment of the SERBP1 sequence (GenBank GENBANK AF151813) with the genomic sequence (GRCh37). ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Jan. 21, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 607378 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed